Ruiz B, Farrés A, Langley E, Masso F, Sánchez S
Departamento de Biotecnología, Instituto de Investigaciones Biomédicas, Universidad Nacional Autónoma de México, Apartado Postal 70228, México D.F. 04510, México.
Lipids. 2001 Mar;36(3):283-9. doi: 10.1007/s11745-001-0719-3.
Penicillium candidum produces and secretes a single extracellular lipase with a monomer molecular weight of 29 kDa. However, this enzyme forms dimers and higher molecular weight aggregates under nondenaturing conditions. The lipase from P. candidum was purified 37-fold using Octyl-Sepharose CL-4B and DEAE-Sephadex columns. The optimal assay conditions for lipase activity were 35 degrees C and pH 9. The lipase was stable in the pH range of 5-6 with a pl of 5.5, but rapid loss of the enzyme activity was observed above 25 degrees C. Tributyrin was found to be the best substrate for the P. candidum lipase, among those tested. Metal ions such as Fe2+ and Cu2+ inhibited enzymatic activity and only Ca2+ was able to slightly enhance lipase activity. Ionic detergents inhibited the activity of the enzyme, whereas nonionic detergents stimulated lipase activity.
白地霉产生并分泌一种单体分子量为29 kDa的胞外脂肪酶。然而，在非变性条件下，这种酶会形成二聚体和更高分子量的聚集体。使用辛基琼脂糖凝胶CL-4B和DEAE-葡聚糖凝胶柱对白地霉脂肪酶进行了37倍的纯化。脂肪酶活性的最佳测定条件是35℃和pH 9。该脂肪酶在pH值5-6范围内稳定，其等电点为5.5，但在25℃以上酶活性迅速丧失。在所测试的底物中，三丁酸甘油酯被发现是白地霉脂肪酶的最佳底物。Fe2+和Cu2+等金属离子会抑制酶活性，只有Ca2+能够略微增强脂肪酶活性。离子型去污剂会抑制该酶的活性，而非离子型去污剂则会刺激脂肪酶活性。
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